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Yorodumi- PDB-2lg1: Solution structure of the human AKAP13 PH domain and stabilizing ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lg1 | ||||||
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Title | Solution structure of the human AKAP13 PH domain and stabilizing DH helix | ||||||
Components | A-kinase anchor protein 13 | ||||||
Keywords | METAL BINDING PROTEIN | ||||||
Function / homology | Function and homology information regulation of sarcomere organization / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / regulation of Rho protein signal transduction / MAP-kinase scaffold activity / cardiac muscle cell differentiation / regulation of small GTPase mediated signal transduction / NRAGE signals death through JNK / RHOB GTPase cycle / protein kinase A binding / positive regulation of Rho protein signal transduction ...regulation of sarcomere organization / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / regulation of Rho protein signal transduction / MAP-kinase scaffold activity / cardiac muscle cell differentiation / regulation of small GTPase mediated signal transduction / NRAGE signals death through JNK / RHOB GTPase cycle / protein kinase A binding / positive regulation of Rho protein signal transduction / adrenergic receptor signaling pathway / RHOC GTPase cycle / RHOA GTPase cycle / bone development / guanyl-nucleotide exchange factor activity / small GTPase binding / G alpha (12/13) signalling events / heart development / cell cortex / positive regulation of canonical NF-kappaB signal transduction / molecular adaptor activity / G protein-coupled receptor signaling pathway / membrane / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Lenoir, M. / Sugawara, M. / Ball, L. / Overduin, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2014 Title: Structural Insights into the Activation of the RhoA GTPase by the Lbc Oncoprotein. Authors: Lenoir, M. / Sugawara, M. / Kaur, J. / Ball, L.J. / Overduin, M. #1: Journal: Biomol.Nmr Assign. / Year: 2009 Title: Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix. Authors: Sugawara, M. / Whittaker, S.B. / Bishop, S. / Ball, L. / Overduin, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lg1.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2lg1.ent.gz | 971.6 KB | Display | PDB format |
PDBx/mmJSON format | 2lg1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lg1_validation.pdf.gz | 555.9 KB | Display | wwPDB validaton report |
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Full document | 2lg1_full_validation.pdf.gz | 3.6 MB | Display | |
Data in XML | 2lg1_validation.xml.gz | 653.3 KB | Display | |
Data in CIF | 2lg1_validation.cif.gz | 420.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lg/2lg1 ftp://data.pdbj.org/pub/pdb/validation_reports/lg/2lg1 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 21055.184 Da / Num. of mol.: 1 / Fragment: PH domain residues 2164-2346 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AKAP13, BRX, HT31, LBC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-Rosetta / References: UniProt: Q12802 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5 mM [U-100% 13C; U-100% 15N] AKAP13a_A10, 50.0 mM sodium phosphate, 150.0 mM sodium chloride, 0.1 mM Sodium azide, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 150 / pH: 7 / Pressure: 1.00 atm / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Varian UnityInova / Manufacturer: Varian / Model: UnityInova / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |